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Metallo-Proteins: Structure, Function and Their Roles in Health and Disease

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: 30 May 2024 | Viewed by 3325

Special Issue Editors


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Guest Editor
Department of Environmental, Biological and Pharmaceutical Science and Technology, Università degli Studi della Campania Luigi Vanvitelli, 81100 Caserta, Italy
Interests: gene regulation; cell signalling; protein interactions; molecular recognition mechanisms in proteins; structure–function relationship in proteins; molecular mechanisms of diseases; cancer; clinical research

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Guest Editor
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania "L. Vanvitelli", 81100 Caserta, Italy
Interests: protein folding; protein and peptide structure, dynamics and function; NMR spectroscopy; protein-metal interactions; protein-protein/ligands interactions, protein misfolding diseases

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Guest Editor
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania "L. Vanvitelli", 81100 Caserta, Italy
Interests: protein structure and dynamics; protein-DNA interactions; metals and metallo-proteins; structural biology; NMR spectroscopy

Special Issue Information

Dear Colleagues,

Metals are known to play fundamental roles in organisms across all domains of life, both as free ions or coupled to proteins. For this reason, their cellular levels are thoroughly controlled by homeostatic mechanisms, with abnormal concentrations being associated with toxicity and the development of a wide range of diseases. In metallo-proteins, the metals are the structural and/or catalytic core needed for these structures to perform their biological activities. Misfolding and aggregation of the metallo-proteins represent the basis of many diseases. A detailed understanding of the native structure, dynamics and function of the metallo-proteins and their alteration will provide new insights into disease mechanisms, but also novel biomarkers and therapeutic targets.

In this context, we propose this Special Issue, whose topics include, but are not limited to:

  • roles of metal ions in metallo-protein folding, stability and functions;
  • roles of metallo-proteins in misfolding diseases;
  • metallomics studies; toxic metals effects;
  • in another lane biomarkers for metallo-protein- associated diseases: screening, diagnosis, treatment response, and prognosis;
  • interventions to prevent or reverse metallo-protein-related diseases.

We invite researchers to submit original articles, communications and reviews to for this Special Issue that address any aspect of metallo-proteins, ranging from an atomic/molecular to a cellular/human level.

Dr. Sabrina Esposito
Dr. Luigi Russo
Dr. Gaetano Malgieri
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • metal-binding proteins: structure, function and properties
  • protein folding and dynamics
  • metal ions exposure, uptake, toxicity
  • coordination complex formation
  • signal transduction
  • molecular recognition
  • abnormal metal-protein complex formations
  • environmental contaminants
  • mechanisms of action and effects on human health
  • metallo-proteins as drug targets

Published Papers (2 papers)

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Research

16 pages, 3317 KiB  
Article
Molecular Dynamic Simulations Reveal the Activation Mechanisms of Oxidation-Induced TRPV1
by Yanyan Chu, Huanhuan Zhang, Mengke Yang and Rilei Yu
Int. J. Mol. Sci. 2023, 24(11), 9553; https://doi.org/10.3390/ijms24119553 - 31 May 2023
Viewed by 1472
Abstract
Transient receptor potential vanilloid 1 (TRPV1), a non-selective cation channel, can be directly activated by oxidants through cysteine modification. However, the patterns of cysteine modification are unclear. Structural analysis showed that the free sulfhydryl groups of residue pairs C387 and C391 were potentially [...] Read more.
Transient receptor potential vanilloid 1 (TRPV1), a non-selective cation channel, can be directly activated by oxidants through cysteine modification. However, the patterns of cysteine modification are unclear. Structural analysis showed that the free sulfhydryl groups of residue pairs C387 and C391 were potentially oxidized to form a disulfide bond, which is expected to be closely related to the redox sensing of TRPV1. To investigate if and how the redox states of C387 and C391 activate TRPV1, homology modeling and accelerated molecular dynamic simulations were performed. The simulation revealed the conformational transfer during the opening or closing of the channel. The formation of a disulfide bond between C387 and C391 leads to the motion of pre-S1, which further propagates conformational change to TRP, S6, and the pore helix from near to far. Residues D389, K426, E685–Q691, T642, and T671 contribute to the hydrogen bond transfer and play essential roles in the opening of the channel. The reduced TRPV1 was inactivated mainly by stabilizing the closed conformation. Our study elucidated the redox state of C387–C391 mediated long-range allostery of TRPV1, which provided new insights into the activation mechanism of TRPV1 and is crucial for making significant advances in the treatment of human diseases. Full article
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13 pages, 1566 KiB  
Article
How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site
by Gaël Giraudon--Colas, Stéphanie Devineau, Laurent Marichal, Elodie Barruet, Andrea Zitolo, Jean-Philippe Renault and Serge Pin
Int. J. Mol. Sci. 2023, 24(4), 3659; https://doi.org/10.3390/ijms24043659 - 11 Feb 2023
Cited by 2 | Viewed by 1518
Abstract
The adsorption of proteins on surfaces has been studied for a long time, but the relationship between the structural and functional properties of the adsorbed protein and the adsorption mechanism remains unclear. Using hemoglobin adsorbed on silica nanoparticles, we have previously shown that [...] Read more.
The adsorption of proteins on surfaces has been studied for a long time, but the relationship between the structural and functional properties of the adsorbed protein and the adsorption mechanism remains unclear. Using hemoglobin adsorbed on silica nanoparticles, we have previously shown that hemoglobin’s affinity towards oxygen increases with adsorption. Nevertheless, it was also shown that there were no significant changes in the quaternary and secondary structures. In order to understand the change in activity, we decided in this work to focus on the active sites of hemoglobin, the heme and its iron. After measuring adsorption isotherms of porcine hemoglobin on Ludox silica nanoparticles, we analyzed the structural modifications of adsorbed hemoglobin by X-ray absorption spectroscopy and circular dichroism spectra in the Soret region. It was found that upon adsorption, there were modifications in the heme pocket environment due to changes in the angles of the heme vinyl functions. These alterations can explain the greater affinity observed. Full article
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